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TitlePiracetam Defines a New Binding Site for Allosteric Modulators of alpha-Amino-3-hydroxy-5-methyl-4-isoxazole-propionic Acid (AMPA) Receptors.
Journal, issue, pagesJ. Med. Chem., Vol. 53, Page 2197-2203, Year 2010
Publish dateFeb 12, 2010 (structure data deposition date)
AuthorsAhmed, A.H. / Oswald, R.E.
External linksJ. Med. Chem. / PubMed:20163115
MethodsX-ray diffraction
Resolution1.752 - 2.122 Å
Structure data

PDB-3lsf:
Piracetam bound to the ligand binding domain of GluA2
Method: X-RAY DIFFRACTION / Resolution: 1.851 Å

PDB-3lsl:
Piracetam bound to the ligand binding domain of GluA2 (flop form)
Method: X-RAY DIFFRACTION / Resolution: 2.122 Å

PDB-3lsw:
Aniracetam bound to the ligand binding domain of GluA3
Method: X-RAY DIFFRACTION / Resolution: 1.752 Å

PDB-3lsx:
Piracetam bound to the ligand binding domain of GluA3
Method: X-RAY DIFFRACTION / Resolution: 2.006 Å

Chemicals

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-PZI:
2-(2-oxopyrrolidin-1-yl)acetamide

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-4MP:
1-(4-METHOXYBENZOYL)-2-PYRROLIDINONE

Source
  • rattus norvegicus (Norway rat)
  • mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN / glutamate receptor / GluR2 / GluA2 / AMPA receptor / neurotransmitter receptor / S1S2 / allosteric modulator / Alternative splicing / Cell junction / Cell membrane / Endoplasmic reticulum / Glycoprotein / Ion transport / Ionic channel / Membrane / Phosphoprotein / Postsynaptic cell membrane / Receptor / RNA editing / Synapse / Transmembrane / Transport / GluR3 / GluA3

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